Expression and tissue localization of renalase, a novel soluble FAD-dependent protein, in reproductive/steroidogenic systems

Zhou, Mingxue; Liang, Tong; Wang, Yifeng; Da, Jin; Wang, Jian; Jia, Ling; Zhang, Shuping

doi:10.1007/s11033-012-2476-0

Cited by 18 publications

(18 citation statements)

References 41 publications

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“…Renalase isoform 1 was originally reported to be predominantly expressed in the proximal tubes and glomerulus of the kidney, but was said to be detectable in cardiac muscle, liver tissue and skeletal muscle [11] and the bias for higher expression in the kidney was later confirmed [53]. However, it has since been shown that isoform 1 transcripts are detectable in nerves, adrenal glands, adipose tissue [51], and that expression is prominent in reproductive tissues [54]. Moreover, the Proteomics DB database reports widespread tissue distribution of renalase isoforms 1 and 2 [55].…”

Section: Tissue Distributionmentioning

confidence: 99%

The catalytic function of renalase: A decade of phantoms

Moran

2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Ten years after the initial identification of human renalase the first genuinely catalytic substrates have been identified. Throughout the prior decade a consensus belief that renalase is produced predominantly by the kidney and catalytically oxidizes catecholamines in order to lower blood pressure and slow the heart has prevailed. This belief was, however, based on fundamentally flawed scientific observations that did not include control reactions to account for the well-known autoxidation of catecholamines in oxygenated solutions. Nonetheless, the initial claims have served as the kernel for a rapidly expanding body of research largely predicated on the belief that catecholamines are substrates for this enzyme. The proliferation of scientific studies pertaining to renalase as a hormone has proceeded unabated despite well-reasoned expressions of dissent that have indicated the deficiencies of the initial observations and other inconsistencies. Our group has very recently identified isomeric forms of β-NAD(P)H as substrates for renalase. These substrates arise from non-specific reduction of β-NAD(P)(+) that forms β-4-dihydroNAD(P) (β-NAD(P)H), β-2-dihydroNAD(P) and β-6-dihydroNAD(P); the latter two being substrates for renalase. Renalase oxidizes these substrates with rate constants that are up to 10(4)-fold faster than any claimed for catecholamines. The electrons harvested are delivered to dioxygen via the enzyme's FAD cofactor forming both H2O2 and β-NAD(P)(+) as products. It would appear that the metabolic purpose of this chemistry is to alleviate the inhibitory effect of β-2-dihydroNAD(P) and β-6-dihydroNAD(P) on primary metabolism dehydrogenase enzymes. The identification of this genuinely catalytic activity for renalase calls for re-evaluation of much of the research of this enzyme, in which definitive links between renalase catecholamine consumption and physiological responses were reported. This article is part of a Special Issue entitled: Physiological enzymology and protein functions.

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Section: Tissue Distributionmentioning

confidence: 99%

The catalytic function of renalase: A decade of phantoms

Moran

2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…Genes expressed selectively or specifically in a certain organ may play crucial physiological and/or functional roles in this particular tissue. Our previous study showed that renalase is predominantly expressed in mice steroidogenic/reproductive systems, including in the ovaries, testes, and adrenal glands, 26 and it is also expressed in mice livers. 27 Although these organs are also involved in cholesterol synthesis and/or metabolism, it is an interesting question whether renalase may be involved in lipid metabolism.…”

Section: Discussionmentioning

confidence: 99%

Valsartan Promoting Atherosclerotic Plaque Stabilization by Upregulating Renalase

Zhou

Liu

et al. 2015

J Cardiovasc Pharmacol Ther

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“…A notable reduction in renalase level in preeclamptic women was observed in the present study when compared to the healthy pregnancies. Previously, it was shown that the manipulation of gonadotropinreleasing hormone (GnRH) might alter the expression of renalase and GnRH antagonists downregulate the renalase secretion [25]. As the placenta has a central role in PE [26], ischemic changes observed during PE possibly accompany low GnRH level and diminish GnRH would facilitate a low level of renalase in pre-eclamptic women.…”

Section: Discussionmentioning

confidence: 99%

Renalase levels and genetic variants are associated with preeclampsia: a hospital based study in Chinese cohort

Li¹,

Huang²,

2020

Preprint

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Background Pre-eclampsia (PE) is a major contributor of maternal and fetal morbidity and mortality. There are many host related biomolecules that regulate the pathophysiology PE. Critical analysis of these parameters is of crucial importance as some of these may be used as prognostic/diagnostic marker of this serious ailment and can be targeted for developing therapeutic measures against the disease. The aim of the current study is to examine the role of renalse in the context PE in a Chinese cohort. Methods A hospital based case control study was designed to investigate role of renalase in PE. 384 Chinese women consisting of subjects with normotensive pregnancy (n = 105), women with PE (n = 121) and healthy pregnancy (n = 158) were included in the study. Serum renalse level was measured in recruited subjects by ELISA. Renalase gene polymorphisms (rs10887800, rs2576178 and rs2296545) were genotyped by PCR-RFLP. Results A higher level of serum renalse in healthy pregnant women compared to controls, whereas, subjects with PE demonstrated a reduced level of this enzyme. Renalse level was negatively correlated with systolic as well as diastolic blood pressure, whereas, a positive association was observed with glomerular filtration rate. Prevalence of homozygous mutant (GG) and minor allele (G) of rs10887800 and rs2576178 polymorphisms were higher in PE patients compared to normotensive pregnant women and healthy controls. Furthermore, association of G-G-C haplotype with susceptibility to PE was observed. Conclusions Low level of renalse may be associated with high risk of PE during pregnancy. Renalase gene polymorphisms (rs10887800 and rs2576178) are correlated with with serum renalase and associated with predisposition to development of PE in Chinese cohort.

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Expression and tissue localization of renalase, a novel soluble FAD-dependent protein, in reproductive/steroidogenic systems

Cited by 18 publications

References 41 publications

The catalytic function of renalase: A decade of phantoms

The catalytic function of renalase: A decade of phantoms

Valsartan Promoting Atherosclerotic Plaque Stabilization by Upregulating Renalase

Renalase levels and genetic variants are associated with preeclampsia: a hospital based study in Chinese cohort

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